One of the most efficient hosts for production of recombinant proteins are prokaryotic host cells. Many therapeutic proteins are being used to treat humans and other higher mammals. Yet in spite of the need for efficient and economic methods to produce such proteins, therapeutic proteins are produced in costly eukaryotic cell systems, e.g., mammalian tissue culture cells, such as CHO cells; insect cells, and yeast cells. The main obstacles to use of prokaryotic production systems are production of insoluble therapeutic proteins in many prokaryotic cells, e.g., E. coli, and failure of prokaryotic cells to provide appropriate post-translation modification of eukaryotic proteins, e.g., glycosylation of eukaryotic proteins. Thus, at present production of therapeutic proteins in prokaryotic hosts must include labor intensive and expensive steps of refolding misfolded proteins, purification of refolded therapeutic proteins and purification of refolded glycosyltransferases. The present invention solves these and other needs.